Complete Amino Acid Sequence of Ostrich (Struthio camelus) Egg‐White Lysozyme, a Goose‐Type Lysozyme
Open Access
- 1 April 1982
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 123 (3), 489-497
- https://doi.org/10.1111/j.1432-1033.1982.tb06557.x
Abstract
The complete amino acid sequence (185 amino acid residues) of the goose-type lysozyme from the egg white of ostrich (Struthio camelus) was determined from the study of tryptic (EC 3.4.21.4) and Staphylococcus aureus V8 protease (EC 3.4.21.19) peptides as well as of CNBr and BNPS-skatole [Br adduct of 2-(2-nitrophenylsulfenyl)-3-methylindole] fragments. A slight sequence homology between the goose-type and chicken-type lysozymes was observed.This publication has 21 references indexed in Scilit:
- Micro‐sequence analysis of peptides and proteins using 4‐NN‐dimethylaminoazobenzene 4′‐isothiocyanate/phenylisothiocyanate double coupling methodFEBS Letters, 1978
- The use of methanol in high‐performance liquid chromatography of phenylthiohydantoin—amino acidsFEBS Letters, 1978
- Structural data concerning reptilian (tortoise) egg lysozymeJournal of Molecular Evolution, 1977
- The Ostrich (Struthio camelus) egg-white lysozymeMolecular and Cellular Biochemistry, 1977
- The Sequence of Sheep κ‐Casein: Primary Structure of para‐κA‐CaseinEuropean Journal of Biochemistry, 1974
- The primary structure of bovine growth hormoneFEBS Letters, 1973
- Application of sequenator analysis to the study of proteinsBiochemistry, 1972
- High temperature crystallization of lysozyme: An example of phase transitionFEBS Letters, 1972
- Étude d'un lysozyme pauvre en cystine et en tryptophane: Le lysozyme de blanc d'oeuf d'oieBiochimica et Biophysica Acta (BBA) - Protein Structure, 1967
- Purification and characterization of a lysozyme from goose egg whiteBiochemical and Biophysical Research Communications, 1967